메뉴 건너뛰기




Volumn 352, Issue 1, 2005, Pages 11-21

A structural basis for depolymerization of alginate by polysaccharide lyase family-7

Author keywords

Active center; Alginate lyase; Crystal structure; Polysaccharide lyase family 7

Indexed keywords

ALGINIC ACID; AMMONIUM SULFATE; ARGININE; GLUTAMINE; HISTIDINE; ISOENZYME; POLYSACCHARIDE LYASE; SULFATE; TYROSINE;

EID: 23944435850     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.06.075     Document Type: Article
Times cited : (101)

References (34)
  • 1
    • 0002702320 scopus 로고    scopus 로고
    • Commercial applications of alginates
    • E. Onsøyen Commercial applications of alginates Carbohydr. Eur. 14 1996 26 31
    • (1996) Carbohydr. Eur. , vol.14 , pp. 26-31
    • Onsøyen, E.1
  • 2
    • 0034142988 scopus 로고    scopus 로고
    • Alginate dressings in surgery and wound management: Part 1
    • S. Thomas Alginate dressings in surgery and wound management: part 1 J. Wound Care 9 2000 56 60
    • (2000) J. Wound Care , vol.9 , pp. 56-60
    • Thomas, S.1
  • 5
    • 0027474289 scopus 로고
    • Promotion of germination and shoot elongation of some plants by alginate oligomers prepared with bacterial alginate lyase
    • Y. Yonemoto, H. Tanaka, T. Yamashita, N. Kitabatake, Y. Ishida, A. Kimura, and K. Murata Promotion of germination and shoot elongation of some plants by alginate oligomers prepared with bacterial alginate lyase J. Ferment. Bioeng. 75 1993 68 70
    • (1993) J. Ferment. Bioeng. , vol.75 , pp. 68-70
    • Yonemoto, Y.1    Tanaka, H.2    Yamashita, T.3    Kitabatake, N.4    Ishida, Y.5    Kimura, A.6    Murata, K.7
  • 6
    • 0037797474 scopus 로고
    • Cystic fibrosis
    • M.E. Hodson A.P. Norman J.C. Batten Oxford University Press London
    • J.C. Batten, and D.J. Matthew Cystic fibrosis M.E. Hodson A.P. Norman J.C. Batten The Respiratory System 1983 Oxford University Press London 105 131
    • (1983) The Respiratory System , pp. 105-131
    • Batten, J.C.1    Matthew, D.J.2
  • 9
    • 0034084571 scopus 로고    scopus 로고
    • Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases
    • H.-J. Yoon, W. Hashimoto, O. Miyake, B. Mikami, and K. Murata Overexpression in Escherichia coli, purification, and characterization of Sphingomonas sp. A1 alginate lyases Protein Expr. Purif. 19 2000 84 90
    • (2000) Protein Expr. Purif. , vol.19 , pp. 84-90
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Mikami, B.4    Murata, K.5
  • 10
    • 0031885464 scopus 로고    scopus 로고
    • Extracellular poly (α-l-guluronate) lyase from Corynebacterium sp.: Purification, characteristics, and conformational properties
    • Y. Matsubara, R. Kawada, K. Iwasaki, T. Oda, and T. Muramatsu Extracellular poly (α-l-guluronate) lyase from Corynebacterium sp.: purification, characteristics, and conformational properties J. Protein Chem. 17 1998 29 36
    • (1998) J. Protein Chem. , vol.17 , pp. 29-36
    • Matsubara, Y.1    Kawada, R.2    Iwasaki, K.3    Oda, T.4    Muramatsu, T.5
  • 11
    • 0027233441 scopus 로고
    • Sequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginate
    • M. Malissard, C. Duez, M. Guinand, M.J. Vacheron, G. Michel, and N. Marty Sequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginate FEMS Microbiol. Letters 110 1993 101 106
    • (1993) FEMS Microbiol. Letters , vol.110 , pp. 101-106
    • Malissard, M.1    Duez, C.2    Guinand, M.3    Vacheron, M.J.4    Michel, G.5    Marty, N.6
  • 12
    • 3843150512 scopus 로고    scopus 로고
    • Structure and function of a hypothetical Pseudomonas aeruginosa protein PA1167 classified into family PL-7
    • M. Yamasaki, S. Moriwaki, O. Miyake, W. Hashimoto, K. Murata, and B. Mikami Structure and function of a hypothetical Pseudomonas aeruginosa protein PA1167 classified into family PL-7 J. Biol. Chem. 279 2004 31863 31872
    • (2004) J. Biol. Chem. , vol.279 , pp. 31863-31872
    • Yamasaki, M.1    Moriwaki, S.2    Miyake, O.3    Hashimoto, W.4    Murata, K.5    Mikami, B.6
  • 13
    • 0033538420 scopus 로고    scopus 로고
    • Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 Å resolution
    • H.-J. Yoon, B. Mikami, W. Hashimoto, and K. Murata Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 Å resolution J. Mol. Biol. 290 1999 505 514
    • (1999) J. Mol. Biol. , vol.290 , pp. 505-514
    • Yoon, H.-J.1    Mikami, B.2    Hashimoto, W.3    Murata, K.4
  • 14
    • 0035896032 scopus 로고    scopus 로고
    • Crystal structure of alginate lyase A1-III complexed with a trisaccharide product at 2.0 Å resolution
    • H.-J. Yoon, W. Hashimoto, O. Miyake, K. Murata, and B. Mikami Crystal structure of alginate lyase A1-III complexed with a trisaccharide product at 2.0 Å resolution J. Mol. Biol. 307 2001 9 16
    • (2001) J. Mol. Biol. , vol.307 , pp. 9-16
    • Yoon, H.-J.1    Hashimoto, W.2    Miyake, O.3    Murata, K.4    Mikami, B.5
  • 15
    • 1442265845 scopus 로고    scopus 로고
    • X-ray structural analysis of alginate lyase A1-III mutants/substrate complexes: Activation of a catalytic tyrosine residue by a flexible lid loop
    • B. Mikami, S. Suzuki, H.-J. Yoon, O. Miyake, W. Hashimoto, and K. Murata X-ray structural analysis of alginate lyase A1-III mutants/substrate complexes: activation of a catalytic tyrosine residue by a flexible lid loop Acta Crystallog. sect. A 58 2002 C271
    • (2002) Acta Crystallog. Sect. a , vol.58 , pp. 271
    • Mikami, B.1    Suzuki, S.2    Yoon, H.-J.3    Miyake, O.4    Hashimoto, W.5    Murata, K.6
  • 16
    • 11844301646 scopus 로고    scopus 로고
    • Crystal structure of the alginate (poly α-l-guluronate) lyase from Corynebacterium sp. at 1.2 Å resolution
    • T. Osawa, Y. Matsubara, T. Muramatsu, M. Kimura, and Y. Kakuta Crystal structure of the alginate (poly α-l-guluronate) lyase from Corynebacterium sp. at 1.2 Å resolution J. Mol. Biol. 345 2005 1111 1118
    • (2005) J. Mol. Biol. , vol.345 , pp. 1111-1118
    • Osawa, T.1    Matsubara, Y.2    Muramatsu, T.3    Kimura, M.4    Kakuta, Y.5
  • 17
    • 0037125998 scopus 로고    scopus 로고
    • Convergent evolution sheds light on the anti-β-elimination mechanism common to family 1 and 10 polysaccharide lyases
    • S.J. Charnock, I.E. Brown, J.P. Turkenburg, G.W. Black, and G.D. Davies Convergent evolution sheds light on the anti-β-elimination mechanism common to family 1 and 10 polysaccharide lyases Proc. Natl Acad. Sci. USA 99 2002 12067 12072
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12067-12072
    • Charnock, S.J.1    Brown, I.E.2    Turkenburg, J.P.3    Black, G.W.4    Davies, G.D.5
  • 18
    • 33645483248 scopus 로고    scopus 로고
    • Origin and diversity of alginate lyases of families PL-5 and PL-7 in Sphingomonas sp. strain A1
    • O. Miyake, A. Ochiai, W. Hashimoto, and K. Murata Origin and diversity of alginate lyases of families PL-5 and PL-7 in Sphingomonas sp. strain A1 J. Bacteriol. 189 2004 2981 2986
    • (2004) J. Bacteriol. , vol.189 , pp. 2981-2986
    • Miyake, O.1    Ochiai, A.2    Hashimoto, W.3    Murata, K.4
  • 19
    • 33645494052 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of alginate lyases A1-II and A1-II′ from Sphingomonas sp. A1
    • M. Yamasaki, K. Ogura, S. Moriwaki, W. Hashimoto, K. Murata, and B. Mikami Crystallization and preliminary X-ray analysis of alginate lyases A1-II and A1-II′ from Sphingomonas sp. A1 Acta Crystallog. sect. F 61 2005 288 290
    • (2005) Acta Crystallog. Sect. F , vol.61 , pp. 288-290
    • Yamasaki, M.1    Ogura, K.2    Moriwaki, S.3    Hashimoto, W.4    Murata, K.5    Mikami, B.6
  • 20
    • 0029645404 scopus 로고
    • Structure and mechanism of glycosyl hydrolases
    • G. Davis, and B. Henrissat Structure and mechanism of glycosyl hydrolases Structure 15 1995 853 859
    • (1995) Structure , vol.15 , pp. 853-859
    • Davis, G.1    Henrissat, B.2
  • 21
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cell cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei
    • C. Divne, J. Ståhlberg, T.T. Teeri, and A. Jones High-resolution crystal structures reveal how a cell cellulose chain is bound in the 50 Å long tunnel of cellobiohydrolase I from Trichoderma reesei J. Mol. Biol. 275 1998 309 325
    • (1998) J. Mol. Biol. , vol.275 , pp. 309-325
    • Divne, C.1    Ståhlberg, J.2    Teeri, T.T.3    Jones, A.4
  • 22
    • 0030833928 scopus 로고    scopus 로고
    • Minimizing nonproductive substrate binding: A new look at glucoamylase subsite affinities
    • S.K. Natarajan, and M.R. Sierks Minimizing nonproductive substrate binding: a new look at glucoamylase subsite affinities Biochemistry 36 1997 14946 14955
    • (1997) Biochemistry , vol.36 , pp. 14946-14955
    • Natarajan, S.K.1    Sierks, M.R.2
  • 24
    • 0031015902 scopus 로고    scopus 로고
    • Nomenclature for sugar-binding subsites in glycosyl hydrolases
    • G.J. Davis, K.S. Wilson, and B. Henrissat Nomenclature for sugar-binding subsites in glycosyl hydrolases Biochem. J. 321 1997 557 559
    • (1997) Biochem. J. , vol.321 , pp. 557-559
    • Davis, G.J.1    Wilson, K.S.2    Henrissat, B.3
  • 25
    • 0037008738 scopus 로고    scopus 로고
    • Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase
    • M.J. Jedrzejas, L.V. Mello, B.L. De Groot, and S. Li Mechanism of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase J. Biol. Chem. 277 2002 28287 28297
    • (2002) J. Biol. Chem. , vol.277 , pp. 28287-28297
    • Jedrzejas, M.J.1    Mello, L.V.2    De Groot, B.L.3    Li, S.4
  • 26
    • 21744444127 scopus 로고    scopus 로고
    • Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: Insights into the enzyme reaction mechanism
    • Y. Maruyama, W. Hashimoto, B. Mikami, and K. Murata Crystal structure of Bacillus sp. GL1 xanthan lyase complexed with a substrate: Insights into the enzyme reaction mechanism J. Mol. Biol. 350 2005 974 986
    • (2005) J. Mol. Biol. , vol.350 , pp. 974-986
    • Maruyama, Y.1    Hashimoto, W.2    Mikami, B.3    Murata, K.4
  • 27
    • 1442323777 scopus 로고    scopus 로고
    • High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: An enzyme-substrate complex defines the catalytic mechanism
    • V.V. Lunin, Y. Li, R.J. Linhardt, H. Miyazono, M. Kyogashima, and T. Kaneko High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism J. Mol. Biol. 337 2004 367 386
    • (2004) J. Mol. Biol. , vol.337 , pp. 367-386
    • Lunin, V.V.1    Li, Y.2    Linhardt, R.J.3    Miyazono, H.4    Kyogashima, M.5    Kaneko, T.6
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0028057108 scopus 로고
    • Raster3D version 2.0. a program for photorealistic molecular graphics
    • A.E. Merritt, and M.E.P. Murphy Raster3D version 2.0. a program for photorealistic molecular graphics Acta Crystallog. sect. D 50 1994 869 873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, A.E.1    Murphy, M.E.P.2
  • 30
    • 0030818593 scopus 로고    scopus 로고
    • PHASE-95: A program package for the processing and analysis of diffraction data from macromolecules
    • W. Furey, and S. Swaminathan PHASE-95: a program package for the processing and analysis of diffraction data from macromolecules Methods Enzymol. 277 1997 590 620
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.